Phosphatidylethanolamine mediates insertion of the catalytic domain of leader peptidase in membranes

FEBS Letters

Demel, Rudy A.¹  Dalbey, Ross E.³  van Klompenburg, Wim¹  von Heijne, Gunnar²  Paetzel, Mark³  de Kruijff, Ben¹  de Jong, Joris M.¹ 

[1] Department Biochemistry of Membranes, Centre for Biomembranes and Lipid Enzymology, Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands;Department of Biochemistry, Arrhenius Laboratory, Stockholm University, S-106 91 Stockholm, Sweden;Department of Chemistry, Ohio State University, Columbus, OH 43210, USA

关键词: Leader peptidase;    Membrane protein;    Protein-lipid interaction;    Protein secretion;    Phosphatidylethanolamine;    Insertion;    CC;    cleavage cassette;    DTT;    dithiothreitol;    LUVETS;    large unilamellar vesicles made by extrusion techniques;    PC;    phosphatidylcholine;    PE;    phosphatidylethanolamine;    PG;    phosphatidylglycerol;    SDS-PAGE;    sodium dodecylsulfate-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(98)00733-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Leader peptidase is an integral membrane protein of E. coli and it catalyses the removal of most signal peptides from translocated precursor proteins. In this study it is shown that when the transmembrane anchors are removed in vivo, the remaining catalytic domain can bind to inner and outer membranes of E. coli. Furthermore, the purified catalytic domain binds to inner membrane vesicles and vesicles composed of purified inner membrane lipids with comparable efficiency. It is shown that the interaction is caused by penetration of a part of the catalytic domain between the lipids. Penetration is mediated by phosphatidylethanolamine, the most abundant lipid in E. coli, and does not seem to depend on electrostatic interactions. A hydrophobic segment around the catalytically important residue serine 90 is required for the interaction with membranes.

【 授权许可】

Unknown